SLAB_DEIAC
ID SLAB_DEIAC Reviewed; 146 AA.
AC Q9DEF8; Q7T2Y3; Q8JIV7; Q98SM5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Snaclec anticoagulant protein subunit B;
DE Short=AaACP-B;
DE AltName: Full=ACF 1/2 B-chain;
DE AltName: Full=Agkisasin-b;
DE Flags: Precursor;
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=12175618; DOI=10.1016/s0041-0101(01)00289-6;
RA Tani A., Ogawa T., Nose T., Nikandrov N.N., Deshimaru M., Chijiwa T.,
RA Chang C.C., Fukumaki Y., Ohno M.;
RT "Characterization, primary structure and molecular evolution of
RT anticoagulant protein from Agkistrodon actus venom.";
RL Toxicon 40:803-813(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Yu H., Xiang K., Wang Y., Liu J.;
RT "B chain of ACF 1/2 from Deinagkistrodon acutus.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 23-146.
RC TISSUE=Venom gland;
RA Zha X.D., Ren B., Liu J., Xu K.S.;
RT "Genomic DNA sequence of b chain of Agkisasin, a C-type lectin-like protein
RT from Agkistrodon acutus venom, and its evolutionary significance.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-152 IN DIMER WITH
RP AGKISACUTACIN-A, METAL-BINDING SITES, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=11404471; DOI=10.1073/pnas.131179698;
RA Mizuno H., Fujimoto Z., Atoda H., Morita T.;
RT "Crystal structure of an anticoagulant protein in complex with the Gla
RT domain of factor X.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7230-7234(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 24-152 IN DIMER WITH
RP AGKISACUTACIN-A AND AAACP-A, METAL-BINDING SITES, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RA Zhu Z., Liu S., Mo X., Yu X., Liang Z., Zang J., Zhao W., Teng M., Niu L.;
RT "Characterizations and crystal structures of two snake venom proteins with
RT the activity of binding coagulation factor X from Agkistrodon acutus.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Anticoagulant protein which binds to the gamma-
CC carboxyglutamic acid-domain regions of factors IX and factor X in the
CC presence of calcium with a 1 to 1 stoichiometry. Also inhibits platelet
CC aggregation by binding to platelet glycoprotein Ibalpha (GP1BA) and
CC functioning as a blocker of vWF. Is devoid of hemorrhagic and lethal
CC activities. Possesses antithrombotic and thrombolytic activities. Also
CC hydrolyzes the Aalpha-chain of fibrinogen. Does not affect the Bbeta-
CC chain and the gamma chain (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with subunit A of agkisacutacin or AaACP;
CC disulfide-linked. {ECO:0000269|PubMed:11404471, ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; AB036881; BAB20441.1; -; mRNA.
DR EMBL; AY091761; AAM22789.1; -; mRNA.
DR EMBL; AF350324; AAK26430.1; -; mRNA.
DR EMBL; AY293866; AAP50528.1; -; Genomic_DNA.
DR PDB; 1IOD; X-ray; 2.30 A; B=24-146.
DR PDB; 1WT9; X-ray; 2.01 A; B=24-146.
DR PDB; 1Y17; X-ray; 2.40 A; B=24-146.
DR PDBsum; 1IOD; -.
DR PDBsum; 1WT9; -.
DR PDBsum; 1Y17; -.
DR AlphaFoldDB; Q9DEF8; -.
DR SMR; Q9DEF8; -.
DR EvolutionaryTrace; Q9DEF8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation cascade inhibiting toxin; Calcium;
KW Disulfide bond; Hemostasis impairing toxin; Metal-binding;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..146
FT /note="Snaclec anticoagulant protein subunit B"
FT /id="PRO_5000049505"
FT DOMAIN 24..146
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 25..36
FT DISULFID 53..142
FT DISULFID 98
FT /note="Interchain (with C-102 in subunit A)"
FT DISULFID 119..134
FT CONFLICT 14
FT /note="L -> V (in Ref. 2; AAM22789)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="A -> G (in Ref. 2; AAM22789)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="A -> M (in Ref. 3; AAK26430)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="P -> L (in Ref. 3; AAK26430/AAP50528)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="S -> G (in Ref. 2; AAM22789)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="K -> N (in Ref. 2; AAM22789 and 3; AAK26430/
FT AAP50528)"
FT /evidence="ECO:0000305"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:1WT9"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1WT9"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1WT9"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1IOD"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:1WT9"
SQ SEQUENCE 146 AA; 16997 MW; 420D71EBE4E9F5D2 CRC64;
MGRFIFVSFG LLVLFLSLSG TAADCPSDWS SYEGHCYKPF NEPKNWADAE NFCTQQHTGS
HLVSFQSTEE ADFVVKLAFQ TFDYGIFWMG LSKIWNQCNW QWSNAAMLKY TDWAEESYCV
YFKSTNNKWR SITCRMIANF VCEFQA
